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PDBsum entry 4i8d

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protein ligands Protein-protein interface(s) links
Hydrolase PDB id
4i8d
Jmol
Contents
Protein chains
711 a.a.
Ligands
NAG-NAG-BMA-MAN-
MAN-MAN-MAN-MAN
×2
NAG
BGC ×2
NAG-NAG-BMA-MAN
Waters ×447
PDB id:
4i8d
Name: Hydrolase
Title: Crystal structure of beta-d-glucoside glucohydrolase from tr reesei
Structure: Beta-d-glucoside glucohydrolase. Chain: a, b. Engineered: yes
Source: Trichoderma reesei. Organism_taxid: 51453. Gene: aaa18473, bgl1. Expressed in: pichia pastoris. Expression_system_taxid: 4922.
Resolution:
2.48Å     R-factor:   0.204     R-free:   0.270
Authors: K.E.Helmich,G.Banerjee,C.M.Bianchetti,M.Gudmundsson,M.Sandgr J.D.Walton,G.N.Phillips Jr.,Center For Eukaryotic Structura Genomics (Cesg)
Key ref: K.E.Helmich et al. Crystal structure of beta-D-Glucoside glucohydrolase trichoderma reesei. To be published, .
Date:
03-Dec-12     Release date:   19-Dec-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q12715  (Q12715_HYPJE) -  Beta-D-glucoside glucohydrolase
Seq:
Struc:
 
Seq:
Struc:
744 a.a.
711 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.2.1.21  - Beta-glucosidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Hydrolysis of terminal, non-reducing beta-D-glucose residues with release of beta-D-glucose.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     hydrolase activity, hydrolyzing O-glycosyl compounds     1 term